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LongText Report for: 6ap7-pdb

Name Class
6ap7-pdb
HEADER    PLANT PROTEIN                           17-AUG-17   6AP7              
TITLE     CRYSTAL STRUCTURE OF DAD2 IN COMPLEX WITH 2-(2-METHYL-3-NITROANILINO) 
TITLE    2 BENZOIC ACID                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE STRIGOLACTONE ESTERASE DAD2;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PROTEIN DECREASED APICAL DOMINANCE 2;                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PETUNIA HYBRIDA;                                
SOURCE   3 ORGANISM_COMMON: PETUNIA;                                            
SOURCE   4 ORGANISM_TAXID: 4102;                                                
SOURCE   5 GENE: DAD2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA GAMI 2;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST566                                  
KEYWDS    ALPHA/BETA HYDROLASE, PLANT PROTEIN                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.HAMIAUX                                                             
REVDAT   1   21-MAR-18 6AP7    0                                                
JRNL        AUTH   C.HAMIAUX,R.S.M.DRUMMOND,Z.LUO,H.W.LEE,P.SHARMA,B.J.JANSSEN, 
JRNL        AUTH 2 N.B.PERRY,W.A.DENNY,K.C.SNOWDEN                              
JRNL        TITL   INHIBITION OF STRIGOLACTONE RECEPTORS BY N-PHENYLANTHRANILIC 
JRNL        TITL 2 ACID DERIVATIVES: STRUCTURAL AND FUNCTIONAL INSIGHTS         
JRNL        REF    J.BIOL.CHEM.                               2018              
JRNL        REFN                   ESSN 1083-351X                               
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.HAMIAUX,R.S.DRUMMOND,B.J.JANSSEN,S.E.LEDGER,J.M.COONEY,    
REMARK   1  AUTH 2 R.D.NEWCOMB,K.C.SNOWDEN                                      
REMARK   1  TITL   DAD2 IS AN ALPHA/BETA HYDROLASE LIKELY TO BE INVOLVED IN THE 
REMARK   1  TITL 2 PERCEPTION OF THE PLANT BRANCHING HORMONE, STRIGOLACTONE.    
REMARK   1  REF    CURR. BIOL.                   V.  22  2032 2012              
REMARK   1  REFN                   ISSN 1879-0445                               
REMARK   1  PMID   22959345                                                     
REMARK   1  DOI    10.1016/J.CUB.2012.08.007                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.51 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0124                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.27                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 66090                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3485                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.51                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.55                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4204                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2800                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 197                          
REMARK   3   BIN FREE R VALUE                    : 0.3040                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4154                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 450                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 10.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.10000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.24000                                              
REMARK   3    B12 (A**2) : 0.12000                                              
REMARK   3    B13 (A**2) : -0.09000                                             
REMARK   3    B23 (A**2) : 0.20000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.081         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.082         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.066         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.628         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4403 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4178 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6002 ; 1.760 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9545 ; 1.436 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   547 ; 5.677 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   205 ;28.059 ;22.585       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   685 ;13.102 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;15.842 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   666 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5075 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1111 ; 0.010 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     3    266       B     3    266   32876 0.090 0.050     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A   266                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.2690 -51.2530 -34.5610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0120 T22:   0.1088                                     
REMARK   3      T33:   0.0103 T12:  -0.0052                                     
REMARK   3      T13:  -0.0017 T23:   0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1828 L22:   1.1100                                     
REMARK   3      L33:   2.0289 L12:   0.4644                                     
REMARK   3      L13:  -0.1150 L23:  -0.9659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0153 S12:  -0.0617 S13:   0.0411                       
REMARK   3      S21:   0.0336 S22:   0.0128 S23:  -0.0366                       
REMARK   3      S31:   0.0199 S32:  -0.0418 S33:   0.0026                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     3        B   266                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.3230 -36.3980 -70.3690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0137 T22:   0.1535                                     
REMARK   3      T33:   0.0168 T12:  -0.0340                                     
REMARK   3      T13:  -0.0111 T23:   0.0415                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3203 L22:   0.8281                                     
REMARK   3      L33:   1.2534 L12:   0.0384                                     
REMARK   3      L13:   0.0404 L23:  -0.2835                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0354 S12:   0.0857 S13:   0.0400                       
REMARK   3      S21:  -0.0491 S22:   0.0076 S23:   0.0533                       
REMARK   3      S31:   0.0338 S32:  -0.0190 S33:   0.0278                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.10                                          
REMARK   3   ION PROBE RADIUS   : 0.70                                          
REMARK   3   SHRINKAGE RADIUS   : 0.70                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 6AP7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229529.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-AUG-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : AIMLESS 0.5.12                     
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69577                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.510                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.83000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.7                                          
REMARK 200 STARTING MODEL: 4DNP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: ROD                                                          
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS/ACETATE 0.1M, MGCL2 0.2M, PEG       
REMARK 280  3350 27%, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ARG A   267                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B   267                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NE2  HIS B   210     O    HOH B   401              1.97            
REMARK 500   O    HOH B   431     O    HOH B   502              2.00            
REMARK 500   O    HOH B   403     O    HOH B   527              2.01            
REMARK 500   OD2  ASP B    61     O    HOH B   402              2.02            
REMARK 500   OD1  ASN B    10     O    HOH B   403              2.03            
REMARK 500   OD1  ASN A    10     O    HOH A   401              2.06            
REMARK 500   O    HOH A   411     O    HOH B   403              2.09            
REMARK 500   O    HOH A   401     O    HOH A   411              2.09            
REMARK 500   O    HOH B   404     O    HOH B   568              2.09            
REMARK 500   O    HOH A   401     O    HOH B   527              2.09            
REMARK 500   O    HOH B   596     O    HOH B   605              2.10            
REMARK 500   OE2  GLU B   148     O    HOH B   404              2.11            
REMARK 500   O    HOH A   401     O    HOH A   555              2.12            
REMARK 500   O    HOH B   401     O    HOH B   610              2.12            
REMARK 500   O    HOH A   401     O    HOH A   542              2.13            
REMARK 500   O    HOH A   401     O    HOH A   522              2.15            
REMARK 500   O    HOH A   463     O    HOH A   544              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  76   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG A 182   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG A 199   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  96     -133.86     54.03                                   
REMARK 500    ARG A 124      119.00   -166.22                                   
REMARK 500    GLU A 129      -75.77    -51.88                                   
REMARK 500    ASN A 150       87.00   -156.05                                   
REMARK 500    ALA A 252       56.94   -141.22                                   
REMARK 500    SER B  96     -132.37     56.32                                   
REMARK 500    ARG B 124      115.60   -172.04                                   
REMARK 500    ASN B 150       86.62   -159.08                                   
REMARK 500    ALA B 252       56.70   -142.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BNY A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BNY B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DNP   RELATED DB: PDB                                   
REMARK 900 4DNP IS THE APO PROETIN                                              
DBREF  6AP7 A    1   267  UNP    J9U5U9   DAD2_PETHY       1    267             
DBREF  6AP7 B    1   267  UNP    J9U5U9   DAD2_PETHY       1    267             
SEQADV 6AP7 GLY A   -1  UNP  J9U5U9              EXPRESSION TAG                 
SEQADV 6AP7 GLY A    0  UNP  J9U5U9              EXPRESSION TAG                 
SEQADV 6AP7 GLN A   89  UNP  J9U5U9    CYS    89 ENGINEERED MUTATION            
SEQADV 6AP7 GLY B   -1  UNP  J9U5U9              EXPRESSION TAG                 
SEQADV 6AP7 GLY B    0  UNP  J9U5U9              EXPRESSION TAG                 
SEQADV 6AP7 GLN B   89  UNP  J9U5U9    CYS    89 ENGINEERED MUTATION            
SEQRES   1 A  269  GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL          
SEQRES   2 A  269  ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA          
SEQRES   3 A  269  HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE          
SEQRES   4 A  269  LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR          
SEQRES   5 A  269  ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE          
SEQRES   6 A  269  ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP          
SEQRES   7 A  269  ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP GLN          
SEQRES   8 A  269  CYS ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY          
SEQRES   9 A  269  ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS          
SEQRES  10 A  269  LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP          
SEQRES  11 A  269  GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU          
SEQRES  12 A  269  LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP          
SEQRES  13 A  269  VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL          
SEQRES  14 A  269  PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN          
SEQRES  15 A  269  MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL          
SEQRES  16 A  269  PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS          
SEQRES  17 A  269  VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER          
SEQRES  18 A  269  VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU          
SEQRES  19 A  269  GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY          
SEQRES  20 A  269  HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN          
SEQRES  21 A  269  GLU LEU ARG ARG ALA LEU SER HIS ARG                          
SEQRES   1 B  269  GLY GLY MET GLY GLN THR LEU LEU ASP ALA LEU ASN VAL          
SEQRES   2 B  269  ARG VAL VAL GLY SER GLY GLU ARG VAL LEU VAL LEU ALA          
SEQRES   3 B  269  HIS GLY PHE GLY THR ASP GLN SER ALA TRP ASN ARG ILE          
SEQRES   4 B  269  LEU PRO PHE PHE LEU ARG ASP TYR ARG VAL VAL LEU TYR          
SEQRES   5 B  269  ASP LEU VAL CYS ALA GLY SER VAL ASN PRO ASP PHE PHE          
SEQRES   6 B  269  ASP PHE ARG ARG TYR THR THR LEU ASP PRO TYR VAL ASP          
SEQRES   7 B  269  ASP LEU LEU HIS ILE LEU ASP ALA LEU GLY ILE ASP GLN          
SEQRES   8 B  269  CYS ALA TYR VAL GLY HIS SER VAL SER ALA MET ILE GLY          
SEQRES   9 B  269  ILE LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER LYS          
SEQRES  10 B  269  LEU ILE LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP          
SEQRES  11 B  269  GLU ASP TYR HIS GLY GLY PHE GLU GLN GLY GLU ILE GLU          
SEQRES  12 B  269  LYS VAL PHE SER ALA MET GLU ALA ASN TYR GLU ALA TRP          
SEQRES  13 B  269  VAL ASN GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL          
SEQRES  14 B  269  PRO ALA ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN          
SEQRES  15 B  269  MET ARG PRO ASP ILE THR LEU PHE VAL SER ARG THR VAL          
SEQRES  16 B  269  PHE ASN SER ASP MET ARG GLY VAL LEU GLY LEU VAL LYS          
SEQRES  17 B  269  VAL PRO CYS HIS ILE PHE GLN THR ALA ARG ASP HIS SER          
SEQRES  18 B  269  VAL PRO ALA SER VAL ALA THR TYR LEU LYS ASN HIS LEU          
SEQRES  19 B  269  GLY GLY LYS ASN THR VAL HIS TRP LEU ASN ILE GLU GLY          
SEQRES  20 B  269  HIS LEU PRO HIS LEU SER ALA PRO THR LEU LEU ALA GLN          
SEQRES  21 B  269  GLU LEU ARG ARG ALA LEU SER HIS ARG                          
HET    BNY  A 300      20                                                       
HET    BNY  B 301      20                                                       
HET    GOL  B 302       6                                                       
HETNAM     BNY 2-[(2-METHYL-3-NITROPHENYL)AMINO]BENZOIC ACID                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  BNY    2(C14 H12 N2 O4)                                             
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *450(H2 O)                                                    
HELIX    1 AA1 GLN A    3  LEU A    9  1                                   7    
HELIX    2 AA2 ASP A   30  ASN A   35  5                                   6    
HELIX    3 AA3 ILE A   37  PHE A   41  5                                   5    
HELIX    4 AA4 ASN A   59  PHE A   63  5                                   5    
HELIX    5 AA5 LEU A   71  GLY A   86  1                                  16    
HELIX    6 AA6 SER A   96  ARG A  109  1                                  14    
HELIX    7 AA7 GLU A  136  ASN A  150  1                                  15    
HELIX    8 AA8 ASN A  150  GLY A  164  1                                  15    
HELIX    9 AA9 VAL A  167  MET A  181  1                                  15    
HELIX   10 AB1 ARG A  182  ASN A  195  1                                  14    
HELIX   11 AB2 MET A  198  VAL A  205  5                                   8    
HELIX   12 AB3 PRO A  221  LEU A  232  1                                  12    
HELIX   13 AB4 LEU A  247  ALA A  252  1                                   6    
HELIX   14 AB5 ALA A  252  HIS A  266  1                                  15    
HELIX   15 AB6 THR B    4  LEU B    9  1                                   6    
HELIX   16 AB7 ASP B   30  ASN B   35  5                                   6    
HELIX   17 AB8 ILE B   37  PHE B   41  5                                   5    
HELIX   18 AB9 ASN B   59  PHE B   63  5                                   5    
HELIX   19 AC1 LEU B   71  LEU B   85  1                                  15    
HELIX   20 AC2 SER B   96  ARG B  109  1                                  14    
HELIX   21 AC3 GLU B  136  ASN B  150  1                                  15    
HELIX   22 AC4 ASN B  150  GLY B  164  1                                  15    
HELIX   23 AC5 VAL B  167  MET B  181  1                                  15    
HELIX   24 AC6 ARG B  182  SER B  196  1                                  15    
HELIX   25 AC7 MET B  198  VAL B  205  5                                   8    
HELIX   26 AC8 PRO B  221  LEU B  232  1                                  12    
HELIX   27 AC9 LEU B  247  ALA B  252  1                                   6    
HELIX   28 AD1 ALA B  252  HIS B  266  1                                  15    
SHEET    1 AA1 7 ARG A  12  VAL A  14  0                                        
SHEET    2 AA1 7 TYR A  45  TYR A  50 -1  O  VAL A  47   N  VAL A  14           
SHEET    3 AA1 7 ARG A  19  ALA A  24  1  N  ARG A  19   O  ARG A  46           
SHEET    4 AA1 7 CYS A  90  HIS A  95  1  O  VAL A  93   N  VAL A  22           
SHEET    5 AA1 7 PHE A 113  ILE A 119  1  O  ILE A 117   N  TYR A  92           
SHEET    6 AA1 7 CYS A 209  ALA A 215  1  O  PHE A 212   N  LEU A 118           
SHEET    7 AA1 7 ASN A 236  GLU A 244  1  O  THR A 237   N  ILE A 211           
SHEET    1 AA2 7 ARG B  12  VAL B  14  0                                        
SHEET    2 AA2 7 TYR B  45  TYR B  50 -1  O  LEU B  49   N  ARG B  12           
SHEET    3 AA2 7 ARG B  19  ALA B  24  1  N  ARG B  19   O  ARG B  46           
SHEET    4 AA2 7 CYS B  90  HIS B  95  1  O  VAL B  93   N  ALA B  24           
SHEET    5 AA2 7 PHE B 113  ILE B 119  1  O  ILE B 117   N  TYR B  92           
SHEET    6 AA2 7 CYS B 209  ALA B 215  1  O  PHE B 212   N  LEU B 118           
SHEET    7 AA2 7 ASN B 236  GLU B 244  1  O  HIS B 239   N  ILE B 211           
SITE     1 AC1 14 PHE A  27  SER A  96  PHE A 125  PHE A 135                    
SITE     2 AC1 14 ILE A 140  VAL A 143  PHE A 158  SER A 190                    
SITE     3 AC1 14 VAL A 193  HIS A 218  SER A 219  HIS A 246                    
SITE     4 AC1 14 HOH A 518  HOH A 530                                          
SITE     1 AC2 14 PHE B  27  SER B  96  PHE B 125  PHE B 135                    
SITE     2 AC2 14 ILE B 140  VAL B 143  PHE B 158  SER B 190                    
SITE     3 AC2 14 VAL B 193  HIS B 218  SER B 219  HIS B 246                    
SITE     4 AC2 14 HOH B 579  HOH B 583                                          
SITE     1 AC3  7 THR A 226  LYS A 229  ASN A 230  TYR B 131                    
SITE     2 AC3  7 HIS B 132  SER B 223  HOH B 440                               
CRYST1   36.697   48.315   71.942  82.67  86.76  69.95 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.027250 -0.009945 -0.000398        0.00000                         
SCALE2      0.000000  0.022033 -0.002558        0.00000                         
SCALE3      0.000000  0.000000  0.014016        0.00000                         
TER    2120      HIS A 266                                                      
TER    4244      HIS B 266                                                      
MASTER      389    0    3   28   14    0   10    6 4650    2   46   42          
END                                                                             

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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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